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Tubulin-zinc interactions: binding and polymerization studies.

G R Eagle, R R Zombola, R H Himes

    Biochemistry
    |January 4, 1983
    PubMed
    Summary

    Zinc ions (Zn2+) bind to tubulin, promoting its assembly into various structures. This binding directly influences protein structure and assembly, independent of GTP, revealing a novel mechanism for tubulin regulation.

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    Nucleoside triphosphate specificity of tubulin.

    Biochemistry·2000

    Area of Science:

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Background:

    • Tubulin is the primary protein subunit of microtubules, essential for cell structure and division.
    • The assembly of tubulin is a complex process regulated by various ions and molecules.
    • Understanding tubulin's interaction with divalent cations like Zn2+ is crucial for elucidating microtubule dynamics.

    Purpose of the Study:

    • To investigate the binding characteristics of Zn2+ to tubulin.
    • To determine the role of Zn2+ in promoting tubulin assembly.
    • To clarify the mechanism by which Zn2+ influences tubulin polymorphic assembly.

    Main Methods:

    • Equilibrium binding assays were performed to quantify Zn2+ binding sites on tubulin dimers.
    • Phosphocellulose was used to separate weakly and strongly bound Zn2+.
    • Tubulin assembly was induced and analyzed under various conditions of Zn2+, GTP, Mg2+, and dimethyl sulfoxide (Me2SO).

    Main Results:

    • Tubulin possesses over 60 potential Zn2+ binding sites, with 6-7.5 high-affinity sites per dimer.
    • Zn2+ binding and high-affinity site occupancy increased with incubation time, suggesting slow denaturation.
    • Zn2+ directly stimulates tubulin assembly into protofilament sheets and microtubules, with assembly dependent on Zn2+ concentration and the presence of Mg2+ and Me2SO.

    Conclusions:

    • Zn2+ directly binds to tubulin and promotes its assembly, independent of a ZnGTP complex.
    • The interaction involves direct binding to the protein, potentially leading to conformational changes that favor assembly.
    • This study reveals a direct role for Zn2+ in modulating tubulin structure and microtubule formation.

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